Cleavage by trypsin and by the proteinase from Armillaria mellea at epsilon-N-formyl-lysine residues.
Kinetic studies were made of the hydrolysis by trypsin of alpha-N-acetylglycyl-L-lysine methyl ester and of its neutral analogue alpha-N-acetylglycyl-epsilon-N-formyl-L-lysine methyl ester. The latter substance is a moderately good substrate for trypsin, and this observation is discussed in terms of the substrate specifically of the enzyme. The actions of trypsin and of the lysine-specific proteinase from Armillaria mellea on both a native and a formylated polypeptide substrate were compared. Both enzymes were found to hydrolyse specifically bonds to epsilon-N-formyl-lysine in the formylated substrate.
D000363:Agaricales / Q000201:enzymology*; D004151:Dipeptides / Q000378:metabolism; D010450:Endopeptidases / Q000378:metabolism*; D006868:Hydrolysis; D007700:Kinetics; D008239:Lysine / Q000031:analogs & derivatives* / Q000378:metabolism; D008555:Melitten / Q000378:metabolism; D010446:Peptide Fragments / Q000032:analysis; D014357:Trypsin / Q000378:metabolism*
D004151:Dipeptides; D010446:Peptide Fragments; C020334:N(epsilon)-formyllysine; D008555:Melitten; D010450:Endopeptidases; D014357:Trypsin; D008239:Lysine